› 4zly

X-ray diffraction
1.65Å resolution

Crystal Structure of Bruton's Tyrosine Kinase bound to a Cinnoline Fragment

Released:
DOI: 10.2210/pdb4zly/pdb
PDB entry 4zly coloured by chain, front view.
PDB entry 4zly coloured by chain, side view.
PDB entry 4zly coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Fragment-Based Discovery of a Small Molecule Inhibitor of Bruton's Tyrosine Kinase.
Smith CR, Dougan DR, Komandla M, Kanouni T, Knight B, Lawson JD, Sabat M, Taylor ER, Vu P, Wyrick C
J Med Chem 58 5437-44 (2015)
PMID: 26087137

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170299 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase BTK Chain: A
Molecule details ›
Chain: A
Length: 270 amino acids
Theoretical weight: 31.51 KDa
Source organism: Homo sapiens
Expression system: unidentified baculovirus
UniProt:
  • Canonical: Q06187 (Residues: 389-658; Coverage: 41%)
Gene names: AGMX1, ATK, BPK, BTK
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand IMD 2 x IMD
Ligand IPA 1 x IPA
Ligand DMS 1 x DMS
Ligand 4RU 1 x 4RU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P21212
Unit cell:
a: 72.864Å b: 104.458Å c: 38.047Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.163 0.196
Expression system: unidentified baculovirus

Quick links

Citations

8 review citations

Water in protein hydration and ligand recognition.
Maurer et al. (2019)
7 more

1 mention without citation

Cosolvent Simulations with Fragment-Bound Proteins Identify Hot Spots to Direct Lead Growth.
Lal Gupta et al. (2022)